• DRAMP ID

    • DRAMP00028
    • Peptide Name

    • Lantibiotic epidermin (Bacteriocin)
    • Source

    • Staphylococcus epidermidis TU 3298 / DSM 3095 (Gram-positive bacteria)
    • Family

    • Belongs to the type A lantibiotic family (Class I bacteriocin)
    • Gene

    • epiA
    • Sequence

    • IASKFICTPGCAKTGSFNSYCC
    • Sequence Length

    • 22
    • Protein Existence

    • Protein level
    • Biological Activity

    • Antimicrobial, Antibacterial
    • Target Organism

    • No MICs found in DRAMP database
    • Hemolytic Activity

      • No hemolysis information or data found in the reference(s) presented in this entry
    • Cytotoxicity

      • Not included yet
    • Binding Target

    • Lipid II
    • Linear/Cyclic

    • Not included yet
    • N-terminal Modification

    • Not included yet
    • C-terminal Modification

    • Not included yet
    • Nonterminal Modifications and Unusual Amino Acids

    • Not included yet
    • Stereochemistry

    • Not included yet
    • Structure

    • Rich
    • Structure Description

    • Not found
    • Helical Wheel Diagram

    • DRAMP00028 helical wheel diagram
    • PDB ID

    • None
    • Predicted Structure

    • There is no predicted structure for DRAMP00028.
    • Formula

    • C99H153N25O30S4
    • Absent Amino Acids

    • DEHLMQRVW
    • Common Amino Acids

    • C
    • Mass

    • 2301.69
    • PI

    • 8.52
    • Basic Residues

    • 2
    • Acidic Residues

    • 0
    • Hydrophobic Residues

    • 6
    • Net Charge

    • +2
    • Boman Index

    • -6.8
    • Hydrophobicity

    • 0.427
    • Aliphatic Index

    • 44.55
    • Half Life

      • Mammalian:20 hour
      • Yeast:30 min
      • E.coli:>10 hour
    • Extinction Coefficient Cystines

    • 1740
    • Absorbance 280nm

    • 82.86
    • Polar Residues

    • 13

DRAMP00028

DRAMP00028 chydropathy plot
    • Function

    • Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores.
    • PTM

    • There are one didehydrobutyrine (T14), two lanthionines (S3-C7; S16-C21) and one Beta-methyllanthionine (T8-C11) and one S-(2-aminovinyl)-D-cysteine (S19-C22).
  • ·Literature 1
    • Title

    • Prepeptide sequence of epidermin, a ribosomally synthesized antibiotic with four sulphide-rings.
    • Reference

    • Nature. 1988 May 19;333(6170):276-268.
    • Author

    • Schnell N, Entian KD, Schneider U, Götz F, Zähner H, Kellner R, Jung G.
  • ·Literature 2
    • Title

    • Epidermin: sequencing of a heterodetic tetracyclic 21-peptide amide antibiotic.
    • Reference

    • Eur J Biochem. 1986 Oct 1;160(1):9-22.
    • Author

    • Allgaier H, Jung G, Werner RG, Schneider U, Zähner H.